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Research Article Free access | 10.1172/JCI114889

A phosphatase activity present in peripheral blood myeloid cells of chronic myelogenous leukemia patients but not normal individuals alters nuclear protein binding to transcriptional enhancers of interferon-inducible genes.

D C Seong, S Sims, E Johnson, O M Howard, B Reiter, J Hester, M Talpaz, H Kantarjian, and A Deisseroth

Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Department of Hematology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

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Published November 1, 1990 - More info

Published in Volume 86, Issue 5 on November 1, 1990
J Clin Invest. 1990;86(5):1664–1670. https://doi.org/10.1172/JCI114889.
© 1990 The American Society for Clinical Investigation
Published November 1, 1990 - Version history
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Abstract

Cytoplasmic protein from peripheral blood myeloid cells of chronic myelogenous leukemia (CML) patients altered the electrophoretic mobility of complexes formed between nuclear proteins and interferon-inducible transcriptional enhancers. Immature myeloid marrow cells (blasts and promyelocytes) have a higher level of this activity than do mature myeloid marrow cells (bands and polys). This activity, which is not detectable in the peripheral blood cells of normal individuals, is at least 50-fold higher in CML marrow blasts and promyelocytes than that found in marrow blasts and promyelocytes of normal individuals. This activity was inhibited by in vivo incubation of immature myeloid cells with the phosphatase inhibitor, sodium orthovanadate (0.2 mM), and by adding orthovanadate (20 mM) directly to cytoplasmic proteins of myeloid cells. Interferon-alpha (1,000 U/ml) reduced the effects of the CML myeloid cell cytoplasmic protein on the electrophoretic mobility of nuclear protein-DNA complexes. These data suggest that a unique phosphatase may be involved in the abnormalities in CML which are modulated by interferon-alpha.

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